Information on EC 3.4.24.B17 - FtsH endopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B17
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
FtsH endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
171904-23-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain ATCC 13032
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Manually annotated by BRENDA team
strain AR5771
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Manually annotated by BRENDA team
K12
SwissProt
Manually annotated by BRENDA team
strain TYE024
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Manually annotated by BRENDA team
serovar typhimurium
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-manno-octulosonate transferase + H2O
?
show the reaction diagram
-
3-deoxy-D-manno-octulosonate transferase carries out the attachment of two KDO residues to the lipid A precursor (lipid IVA) to form the minimal essential structure of the lipopolysaccharide (KDO2-lipid A). Thus, FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of lipopolysaccharide
-
-
?
alpha-casein + H2O
?
show the reaction diagram
apo-flavodoxin + H2O
?
show the reaction diagram
-
degradation of apo-flavodoxin from Escherichia coli, no degradation of holo-flavodoxin containing non-covalently bound flavin mononucleotide. A mutant flavodoxin carrying a substitution of Tyr94 to Asp (FldYD) with a lower affinity for FMN is efficiently degraded. FtsH is able to initiate degradation of the FldYD moiety even when it is sandwiched by glutathione S-transferase, green fluorescent protein, or both green fluorescent protein and glutathione S-transferase
-
-
?
ATP + H2O
?
show the reaction diagram
bacteriophage lambdaCII repressor protein + H2O
?
show the reaction diagram
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-
-
-
?
barnase tagged with SsrA tail + H2O
?
show the reaction diagram
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tail specific degradation
-
?
beta-casein + H2O
?
show the reaction diagram
beta-casein + H2O
small peptides of 13-20 amino acid residues
show the reaction diagram
-
-
product analysis
?
biotin carboxylase/biotin carboxyl carrier protein + H2O
?
show the reaction diagram
-
-
-
-
?
BODIPY-casein + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
casein + H2O
peptides
show the reaction diagram
-
-
-
?
chimeric protein PhoA-TM8-C30 + H2O
?
show the reaction diagram
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recombinant substrate protein consists of one transmembrane segment of protein SecY, i.e. TM8, plus the following 30 residues of a cytoplasmic part, and the C-terminal end of alkaline phosphatase PhoA
-
?
CII protein of phage lambda + H2O
?
show the reaction diagram
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-
-
?
colicin D + H2O
?
show the reaction diagram
colicin E3 + H2O
?
show the reaction diagram
conserved hypothetical protein NCgl1985 + H2O
?
show the reaction diagram
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-
-
-
?
dihydrofolate reductase tagged with SsrA tail + H2O
?
show the reaction diagram
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tail specific degradation
-
?
doxorubicin resistance protein B + H2O
?
show the reaction diagram
F0a protein + H2O
?
show the reaction diagram
F0a subunit of the ATP synthetase + H2O
?
show the reaction diagram
-
-
-
-
?
FeoB protein + H2O
?
show the reaction diagram
-
-
-
-
?
FGH-(NO2)FFAF-methyl ester + H2O
FGH-(NO2)F + Phe-Ala-Phe-methyl ester
show the reaction diagram
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exclusively cleaved at the (NO2)Phe-Phe bond
-
?
flavodoxin + H2O
?
show the reaction diagram
FtsZ protein + H2O
?
show the reaction diagram
-
-
-
-
?
fusion protein SecY-(P5)-PhoA + H2O
?
show the reaction diagram
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recombinant substrate protein consists of one protein SecY without its C-terminus, and the alkaline phosphatase PhoA
-
?
glutamate binding protein + H2O
?
show the reaction diagram
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-
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
?
show the reaction diagram
-
-
-
-
?
heat shock sigma factor RpoH (sigma32) + H2O
?
show the reaction diagram
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in addition to the turnover element in region 2.1, a second region important for proteolysis of RpoH by FtsH lies in region C of the sigma factor
-
-
?
heat shock transcription factor sigma32 protein + H2O
?
show the reaction diagram
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-
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?
homocysteine methyltransferase + H2O
?
show the reaction diagram
-
-
-
-
?
isocitrate lyase + H2O
?
show the reaction diagram
-
-
-
-
?
lambda protein CII + H2O
?
show the reaction diagram
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cytoplasmic regulatory protein
-
?
lambda Xis + H2O
?
show the reaction diagram
-
protein substrate is required for site-specific excision of phage lambda from the bacterial chromosome
-
?
largely unfolded alpha-lactalbumin + H2O
peptides
show the reaction diagram
no activity with the native protein, cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
?
LpxC + H2O
?
show the reaction diagram
LpxC protein + H2O
?
show the reaction diagram
malate synthase + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
phage lambda CII protein + H2O
small peptides
show the reaction diagram
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enzyme participates in the phage lambda lysis-lysogeny decision by degrading the CII transcriptional activator and by its response to inhibition by the lambda CIII gene product
-
?
phage lambda CII protein + H2O
small peptides of 13-20 amino acid residues
show the reaction diagram
-
recombinant protein substrate with -terminal or C-terminal His-tag, respectively, or no His-tag
product analysis
?
phage shock protein C + H2O
?
show the reaction diagram
PhoA protein + H2O
?
show the reaction diagram
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-
-
?
Protein + H2O
?
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
protein D1 + H2O
?
show the reaction diagram
protein D2 + H2O
?
show the reaction diagram
protein F0 subunit a + H2O
?
show the reaction diagram
protein F0a + H2O
?
show the reaction diagram
protein FtsZ + H2O
?
show the reaction diagram
protein GgpS + H2O
?
show the reaction diagram
protein GlnK + H2O
?
show the reaction diagram
protein KdtA + H2O
?
show the reaction diagram
protein lambdaCII + H2O
?
show the reaction diagram
protein lambdaCIII + H2O
?
show the reaction diagram
protein lambdaXis + H2O
?
show the reaction diagram
protein LpxC + H2O
?
show the reaction diagram
protein MgtC + H2O
?
show the reaction diagram
protein P22 Arc repressor tagged with 108 motif tail + H2O
?
show the reaction diagram
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tail specific degradation
-
?
protein P22 Arc repressor tagged with SsrA tail + H2O
?
show the reaction diagram
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tail specific degradation
-
?
protein RpoH + H2O
?
show the reaction diagram
protein SecY + H2O
?
show the reaction diagram
protein sigma 32 + H2O
?
show the reaction diagram
protein sigma32 + H2O
?
show the reaction diagram
protein sigma32 + H2O
peptides
show the reaction diagram
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regulatory protein
approximately 10 peptides with MW below 3 kDa
?
protein Spo0M + H2O
?
show the reaction diagram
protein translocation subunit SecY + H2O
?
show the reaction diagram
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-
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-
?
protein YccA + H2O
?
show the reaction diagram
PspC protein + H2O
?
show the reaction diagram
RpoH protein + H2O
?
show the reaction diagram
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enzyme recognizes the internal RpoH protein region, N- and C-terminus have no or only marginal effect on substrate binding
-
?
SecY protein + H2O
?
show the reaction diagram
sigma32 + H2O
?
show the reaction diagram
SoxS + H2O
?
show the reaction diagram
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-
-
-
?
subunit a of F0 + H2O
?
show the reaction diagram
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F0 part of the proton ATPase
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?
subunit alpha of ATPase F0F1 + H2O
?
show the reaction diagram
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-
-
?
succinate dehydrogenase A + H2O
?
show the reaction diagram
-
-
-
-
?
succinate dehydrogenase B + H2O
?
show the reaction diagram
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-
-
-
?
succinate dehydrogenase CD + H2O
?
show the reaction diagram
-
-
-
-
?
superoxide response protein + H2O
?
show the reaction diagram
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase + H2O
?
show the reaction diagram
uncomplexed form of the subunit alpha of the proton ATPase F0 + H2O
?
show the reaction diagram
unfolded alpha-casein + H2O
peptides
show the reaction diagram
-
between 10 and 30 kDa, no large intermediates
?
unfolded pepsin + H2O
peptides
show the reaction diagram
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
?
unstable derivatives of the N-terminal domain of the lambdacI repressor + H2O
?
show the reaction diagram
3 derivatives with a nonpolar pentapeptide tail, i.e. cI104, cI105, cI108, and 1 with the SsrAtag, i.e. cI-SsrA
-
?
YccA protein + H2O
?
show the reaction diagram
YccA-(P3)-PhoA + H2O
?
show the reaction diagram
-
recombinant fusion protein
-
?
YfgM protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-manno-octulosonate transferase + H2O
?
show the reaction diagram
-
3-deoxy-D-manno-octulosonate transferase carries out the attachment of two KDO residues to the lipid A precursor (lipid IVA) to form the minimal essential structure of the lipopolysaccharide (KDO2-lipid A). Thus, FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of lipopolysaccharide
-
-
?
colicin D + H2O
?
show the reaction diagram
colicin E3 + H2O
?
show the reaction diagram
doxorubicin resistance protein B + H2O
?
show the reaction diagram
F0a protein + H2O
?
show the reaction diagram
FeoB protein + H2O
?
show the reaction diagram
-
-
-
-
?
lambda Xis + H2O
?
show the reaction diagram
-
protein substrate is required for site-specific excision of phage lambda from the bacterial chromosome
-
?
LpxC + H2O
?
show the reaction diagram
-
ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC
-
-
?
LpxC protein + H2O
?
show the reaction diagram
phage lambda CII protein + H2O
small peptides
show the reaction diagram
-
enzyme participates in the phage lambda lysis-lysogeny decision by degrading the CII transcriptional activator and by its response to inhibition by the lambda CIII gene product
-
?
Protein + H2O
?
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
protein F0 subunit a + H2O
?
show the reaction diagram
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
protein lambdaCII + H2O
?
show the reaction diagram
-
degradation has regulatory function
-
?
protein lambdaCIII + H2O
?
show the reaction diagram
-
degradation has regulatory function
-
?
protein lambdaXis + H2O
?
show the reaction diagram
-
degradation has regulatory function
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?
protein LpxC + H2O
?
show the reaction diagram
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essential for cell viability, enzyme controls the steady-state level of the LpxC protein, which has a key regulatory role in the biosynthesis of lipopolysaccharides
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?
protein SecY + H2O
?
show the reaction diagram
protein sigma32 + H2O
?
show the reaction diagram
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degradation has regulatory function
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?
protein YccA + H2O
?
show the reaction diagram
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degradation of membrane protein, essentially required as a membrane-integrated quality control
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?
PspC protein + H2O
?
show the reaction diagram
SecY protein + H2O
?
show the reaction diagram
sigma32 + H2O
?
show the reaction diagram
-
hydrolyzes about 140 ATP molecules during the degradation of a single molecule of cy2-sigma32. Degradation of sigma32 proceeds from the N-terminus to the C-terminus
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-
?
YccA protein + H2O
?
show the reaction diagram
YfgM protein + H2O
?
show the reaction diagram
-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',3'-dideoxy-ATP
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2',3'-dideoxy-CTP
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2'-deoxy-ATP
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3'-deoxy-ATP
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7-daza-2'-deoxy-ATP
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low activity
ATPalphaS
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low activity
ATPgammaS
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wild-type enzyme and mutants, dependent on protein substrate, low activity
GTP
can substitute for ATP by 19%
UTP
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ineffective substitute for ATP, low activity
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
functional association
Fe2+
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functional association
Mn2+
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functional association
Ni2+
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functional association
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-dinitrophenol
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-
ADP
strong, complete inhibition at equimolar amounts to ATP
ATP
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inhibitory at high concentration in presence of dimethylsulfoxide
carbonyl cyanide-3-chlorophenylhydrazone
-
antagonist of succinate
Dimethylsulfoxide
-
induces conformational changes, stimulates with SecY as substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate
o-phenanthroline
ortho-phenanthroline
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phage lambda CIII protein
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enzyme participates in the phage lambda lysis-lysogeny decision by degrading the CII transcriptional activator and by its response to inhibition by the lambda CIII gene product
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protein SecE
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stabilizes overexpressed SecY against proteolytic degradation by the enzyme, acts a an antagonist
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protein SpoVM
-
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-casein
temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess
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ATP
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ATP-dependent metalloendoprotease belonging to the AAA family (ATPases associated with diverse cellular activities)
dimethylsulfoxid
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induces conformational changes, stimulates with SecY s substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate
Pepsin
temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess
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succinate
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stimulates, antagonist of carbonyl cyanide-3-chlorophenylhydrazone
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.023
ATP
0.104
CTP
-
pH 8.0, 37C
7.3
GTP
-
pH 8.0, 37C
0.023
protein sigma32
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pH 8.0, 42C
-
additional information
additional information
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kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.65
ATP
0.32
CTP
Escherichia coli
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pH 8.0, 37C
0.53 - 6.08
GTP
0.003
protein sigma32
Escherichia coli
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pH 8.0, 42C
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0.0083
sigma32
Escherichia coli
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0036
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purified recombinant refolded enzyme, substrate protein sigma32
0.014
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purified recombinant fusion protein MF5, ATPase activity
0.055
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purified recombinant fusion protein MF4, ATPase activity
0.056
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purified recombinant fusion protein MF3, ATPase activity
0.07
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purified recombinant fusion protein MF2, ATPase activity
0.113
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purified recombinant mutant G230A
0.349
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purified recombinant mutant F228A
0.735
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purified recombinant wild-type enzyme
1.01
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purified recombinant mutant F228E
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at, ambient temperature
30
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assay at
65
ATPase activity, recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
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poor activity at 30C, best at 42C
36 - 70
5% of maximal activity at 36C, 17% of maximal activity at 50C, 63% of maximal activity at 60C, and 67% of maximal activity at 70C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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x * 70000, SDS-PAGE
71000
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x * 71000, SDS-PAGE
additional information
-
the large complexes exhibit either ATPase and protease activity, while smaller ones do not
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 71000, SDS-PAGE
hexamer
homohexamer
multimer
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x * 70000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of a fragment, covering the entire protease domain (residues 405-634), crystals are grown in a buffer solution containing 0.1 M MES (pH 6.0) and 5% PEG8K, at 20C, using vapor-diffusion technique. 2.79 resolution; crystallization of the soluble cytosolic region of FtsH (residues 126-624), crystals are grown in a buffer solution containing 0.1 M Tris-HCl (pH 7.2) and 1% PEG8K, 0.2 mM Zn acetate, 5 mM MgCl2 and 2.5 mM ADP at 20C, using vapor-diffusion technique. 2.79 A resolution
hanging-drop vapour-diffusion method, AAA domain solution: 10 mg/ml protein, 20 mM Tris-HCl, pH 8.5, 50 mM NaCl, 1 mM DTT, precipitant is 1.5 M ammonium sulfate, 2 to 3 days, X-ray structure determination and analysis at about 1.5 A
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X-ray structure determination and analysis at about 1.5 A, molecular modeling
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microbatch methodFtsH is expressed in Escherichia coli as a construct (residues 146-610) lacking the two transmembrane helices and purified
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coiled-coil C-terminus, residues 541-585, as His-tagged peptide
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HiTrapQ column chromatography and Superdex 200 gel filtration
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Ni-NTA agarose column chromatography, and gel filtration
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recombinant enzyme, solubilization by N-lauylsarcosine, refolding in presence of ATP, Mg2+ and Zn2+, and purification to near homogeneity
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recombinant Hi-Myc-tagged enzyme
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recombinant His-Myc-tagged wild-type and mutant enzymes
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recombinant His-Myc-tagged wild-type and mutants
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recombinant His-tagged enzyme from Escherichia coli
recombinant soluble fusion proteins, more than 80% homogeneity
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recombinant tagged AAA-domain, residues 126-398
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recombinant wild-type and mutants
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Hms174(DE3) cells
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expressed in Escherichia coli strain A8926
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expressed in Escherichia coli strain AR5771
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expression of AAA domain residues 126-398 as tagged protein in strain AR5088
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expression of GST-wild-type enzyme fusion protein, expression of coiled-coil structure mutant enzymes, expression of coiled-coil C-terminus, residues 541-585, as His-tagged peptide
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expression of His-Myc-tagged enzyme
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expression of His-Myc-tagged wild-type and mutant enzymes from strain TY024
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expression of maltose-binding fusion proteins in Escherichia coli
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expression of several mutant enzyme forms
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expression of wild-type and mutant from plasmid
expression of wild-type and mutants
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expression of wild-type and mutants as His-Myc-tagged proteins
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expression of wild-type enzyme in Escherichia coli strain AD465 as His-tagged and Myc-tagged protein
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expression of wild-type tagged with His6- and Myc-tag in Escherichia coli
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ftsH gene, expression as His-tagged enzyme in strain BL21(DE3)
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FtsH is expressed in Escherichia coli as a construct (residues 146-610) lacking the two transmembrane helices
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T.ftsH gene, DNA determination and analysis, expression as His-tagged protein in Escherichia coli
the MtStsH protein can efficiently complement lethality of DELTAftsH3::kan mutations in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the absence of proteins FloT and YqfA reduces the level of the septal-localized protease FtsH
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C229F
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ATPase activity is 114% of wild-type activity, protease activity with BODIPY-casein is 47% of wild-type activity, protease activity with Cy3-sigma32 is 22% of wild-type activity
D223K
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ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 10% of wild-type activity, protease activity with Cy3-sigma32 is 5% of wild-type activity
D272N
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ATPase activity is 97% of wild-type activity, protease activity with BODIPY-casein is 81% of wild-type activity
E226A
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ATPase activity is 10% of wild-type activity, protease activity with BODIPY-casein is 11% of wild-type activity
E226K
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ATPase activity is less than 5% of wild-type activity, protease activity with BODIPY-casein is 6% of wild-type activity
E226Q
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ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 18% of wild-type activity, protease activity with Cy3-sigma32 is 17% of wild-type activity
E273A
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ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 8% of wild-type activity, protease activity with Cy3-sigma32 is less than 5% of wild-type activity
E273D
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ATPase activity is 143% of wild-type activity, protease activity with BODIPY-casein is 82% of wild-type activity
E273K
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ATPase activity is less 5% of wild-type activity, protease activity with BODIPY-casein is 7% of wild-type activity
E273Q
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ATPase activity is 68% of wild-type activity, protease activity with BODIPY-casein is 50% of wild-type activity, protease activity with Cy3-sigma32 is 11% of wild-type activity
E415K
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site-directed mutagenesis, mutation of the zinc binding sequence motif, reduced proteolytic activity
F228A
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site-directed point mutation, proteolytically inactive with protein sigma32, but degrades casein, decreased ATPase activity
F228E
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site-directed point mutation, proteolytically inactive mutant, increased ATPase activity
F228K
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site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity
G230A
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site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity
H271D
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ATPase activity is 78% of wild-type activity, protease activity with BODIPY-casein is 39% of wild-type activity, protease activity with Cy3-sigma32 is 20% of wild-type activity
H417A/E418Q/H421A
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the mutant shows 106% ATPase activity compared to the wild type enzyme
K136N
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site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain
L189W
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mutation ftsH102, partial complementation of temperature sensitivity of the ftsH1 mutant at 42C but not other cols-sensitive mutants, overview
L567R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L574A
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L574R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L581R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
M227K
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ATPase activity is 55% of wild-type activity, protease activity with BODIPY-casein is 69% of wild-type activity, protease activity with Cy3-sigma32 is 8% of wild-type activity
S137N
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site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain
T199A
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site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, inactive, no complementation of a deficient mutant strain
T199N
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site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, highly reduced activity, weak complementation of a deficient mutant strain
H417A/E418Q/H421A
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the mutant shows 106% ATPase activity compared to the wild type enzyme
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K198N
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the mutant shows 12% ATPase activity compared to the wild type enzyme
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additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of an in vitro reaction system in which the enzyme is membrane embedded and not solubilized by detergent, two inverted membrane vesicles or proteoliposomes, one bearing the enzyme, the other bearing the substrate protein, are fused, reconstituted enzyme is accessible to proteinase K because the ATPase and protease are exposed outside the vesicles
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recombinant enzyme, solubilization by N-lauylsarcosine, refolding in presence of ATP, Mg2+ and Zn2+, and purification to near homogeneity, the refolded enzyme has properties similar to the overexpressed solubilized one
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